Mouse Midkine Antibody

Midkine (MK; also Retinoid acid-induced differentiation facor) is a secreted heparin-binding member of the very small pleiotrophin family of proteins. Although its predicted MW is 13 kDa, it runs anomalously at 15-17 kDa in SDS-PAGE. MK is strongly expressed in the embryo, but is known to be secreted in the adult by endothelium, preadipocytes, proximal renal tubular epithelium, and CD4⁺ T cells. MK has multiple activities, including the inhibition of regulatory T cell production, the promotion of adipocyte formation, and the induction of chemokine production by smooth muscle, the clustering of Ach receptors on myoblasts, and the migration of embryonic neurons plus neutrophils and macrophages. It has multiple receptors, including heparin and chondroitin sulfate, LRP-1, nucleolin, ALK, and PTP-zeta. Mature mouse midkine is 118 amino acids (aa) in length (aa 23-140). It possesses two distinct domains, an N-terminal domain spanning aa 23-71, and a C-terminal domain that encompasses aa 81-140. The C-terminal domain is further divided into two basic amino acid clusters that bind heparin. There are two splice variants reported for mouse midkine. One shows a deletion of aa 39-103, while another shows a deletion of aa 80-133. Midkine will form a covalent, crosslinked homodimer through the action of tissue type II transglutaminase. Full-length mature mouse MK (aa 23-140) shares 97% and 86% aa sequence with full-length rat and human MK, respectively..